Search Results - "Dix, Samuel R."

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    Allomorphy as a mechanism of post-translational control of enzyme activity by Wood, Henry P., Cruz-Navarrete, F. Aaron, Baxter, Nicola J., Trevitt, Clare R., Robertson, Angus J., Dix, Samuel R., Hounslow, Andrea M., Cliff, Matthew J., Waltho, Jonathan P.

    Published in Nature communications (02-11-2020)
    “…Enzyme regulation is vital for metabolic adaptability in living systems. Fine control of enzyme activity is often delivered through post-translational…”
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    The structure of a major surface antigen SAG19 from Eimeria tenella unifies the Eimeria SAG family by Ramly, Nur Zazarina, Dix, Samuel R., Ruzheinikov, Sergey N., Sedelnikova, Svetlana E., Baker, Patrick J., Chow, Yock-Ping, Tomley, Fiona M., Blake, Damer P., Wan, Kiew-Lian, Nathan, Sheila, Rice, David W.

    Published in Communications biology (19-03-2021)
    “…In infections by apicomplexan parasites including Plasmodium , Toxoplasma gondii , and Eimeria , host interactions are mediated by proteins including families…”
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    Molecular basis of specificity and deamidation of eIF4A by Burkholderia Lethal Factor 1 by Mobbs, George W., Aziz, Adli A., Dix, Samuel R., Blackburn, G. M., Sedelnikova, Sveta E., Minshull, Thomas C., Dickman, Mark J., Baker, Patrick J., Nathan, Sheila, Raih, Mohd Firdaus, Rice, David W.

    Published in Communications biology (28-03-2022)
    “…Burkholderia pseudomallei lethal factor 1 (BLF1) exhibits site-specific glutamine deamidase activity against the eukaryotic RNA helicase, eIF4A, thereby…”
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    Structural basis for high‐affinity adipate binding to AdpC (RPA4515), an orphan periplasmic‐binding protein from the tripartite tricarboxylate transporter (TTT) family in Rhodopseudomonas palustris by Rosa, Leonardo T., Dix, Samuel R., Rafferty, John B., Kelly, David J.

    Published in The FEBS journal (01-12-2017)
    “…The tripartite tricarboxylate transporter (TTT) family is a poorly characterised group of prokaryotic secondary solute transport systems, which employ a…”
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    TssA from Aeromonas hydrophila: expression, purification and crystallographic studies by Dix, Samuel R., Sun, Ruyue, Harris, Matthew J., Batters, Sarah L., Sedelnikova, Svetlana E., Baker, Patrick J., Thomas, Mark S., Rice, David W.

    “…TssA is a core subunit of the type VI secretion system, which is a major player in interspecies competition in Gram‐negative bacteria. Previous studies on…”
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